Abstract
IN the course of some recent work, it became necessary to obtain information on the dry thermal inactivation of trypsin and ribonuclease. A search of the literature indicated that very little work had been done on the dry inactivation of enzymes. In the present experiments, dry samples of these two enzymes were heated in vacuo at temperatures ranging from 160° to 200° C. The inactivation process was found to be irreversible. The values of the thermodynamic parameters ΔH and ΔS were also calculated from the survival data.
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References
Colowick, S. P., and Kaplan, D. D., eds., Methods in Enzymology, 2, 53 (Academic Press, New York, 1955).
Anfinsen, C. B., Redfield, R. R., et al., J. Biol. Chem., 207, 201 (1954).
Stearn, A. E., Adv. Enzymol., 9, 25 (1949).
Woese, C. R., Arch. Biochem. Biophys., 63, 212 (1956).
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MULLANEY, P. Dry Thermal Inactivation of Trypsin and Ribonuclease. Nature 210, 953 (1966). https://doi.org/10.1038/210953a0
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DOI: https://doi.org/10.1038/210953a0
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